等温滴定量热法
配体(生物化学)
生物物理学
化学
计算生物学
量热法
受体
生物化学
生物
热力学
物理
作者
Judith Lanooij,Elwira Smakowska-Luzan
出处
期刊:Methods in molecular biology
日期:2023-11-30
卷期号:: 295-310
标识
DOI:10.1007/978-1-0716-3511-7_22
摘要
The field of plant receptor biology has rapidly expanded in the past three decades. However, the demonstration of direct interaction between receptor-ligand pairs remains a challenge. Identifying and quantifying protein-ligand interactions is crucial for understanding how they regulate certain physiological processes. An important aspect is the quantification of different parameters of the interaction, like binding affinity, kinetics, and ligand specificity that drive the formation of signaling complexes. In this chapter, we discuss Isothermal Titration Calorimetry (ITC) as a label-free technique to measure thermodynamic parameters of ligand binding with high accuracy and reproducibility. We provide a detailed guideline how to design, perform, analyze, and interpret ITC measurements using as an example the interaction between the SCHENGEN3/GASSHO1 (SGN3/GSO1) leucine-rich repeat receptor-like kinase and its sulfated peptide ligand CASPARIAN STRIP INTEGRITY FACTOR 2 (CIF2).
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